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2zat

From Proteopedia

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Revision as of 09:10, 17 October 2018

Crystal structure of a mammalian reductase

Structural highlights

2zat is a 4 chain structure with sequence from Pig. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:	Carbonyl reductase (NADPH), with EC number 1.1.1.184
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DHRS4_PIG] Reduces all-trans-retinal and 9-cis retinal. Can also catalyze the oxidation of all-trans-retinol with NADP as co-factor, but with much lower efficiency. Reduces alkyl phenyl ketones and alpha-dicarbonyl compounds with aromatic rings, such as pyrimidine-4-aldehyde, 3-benzoylpyridine, 4-benzoylpyridine, menadione and 4-hexanoylpyridine. Has no activity towards aliphatic aldehydes and ketones.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Pig heart peroxisomal carbonyl reductase (PerCR) belongs to the short-chain dehydrogenase/reductase family, and its sequence comprises a C-terminal SRL tripeptide, which is a variant of the type 1 peroxisomal targeting signal (PTS1) Ser-Lys-Leu. PerCR is imported into peroxisomes of HeLa cells when the cells are transfected with vectors expressing the enzyme. However, PerCR does not show specific targeting when introduced into the cells with a protein transfection reagent. To understand the structural basis for peroxisomal localization of PerCR, we determined the crystal structure of PerCR. Our data revealed that the C-terminal PTS1 of each subunit of PerCR was involved in intersubunit interactions and was buried in the interior of the tetrameric molecule. These findings indicate that the PTS1 receptor Pex5p in the cytosol recognizes the monomeric form of PerCR whose C-terminal PTS1 is exposed, and that this PerCR is targeted into the peroxisome, thereby forming a tetramer.

Molecular basis for peroxisomal localization of tetrameric carbonyl reductase.,Tanaka N, Aoki K, Ishikura S, Nagano M, Imamura Y, Hara A, Nakamura KT Structure. 2008 Mar;16(3):388-97. PMID:18334214^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Usami N, Ishikura S, Abe H, Nagano M, Uebuchi M, Kuniyasu A, Otagiri M, Nakayama H, Imamura Y, Hara A. Cloning, expression and tissue distribution of a tetrameric form of pig carbonyl reductase. Chem Biol Interact. 2003 Feb 1;143-144:353-61. PMID:12604222
↑ Tanaka N, Aoki K, Ishikura S, Nagano M, Imamura Y, Hara A, Nakamura KT. Molecular basis for peroxisomal localization of tetrameric carbonyl reductase. Structure. 2008 Mar;16(3):388-97. PMID:18334214 doi:10.1016/j.str.2007.12.022

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2zat"

@@ Line 1: / Line 1: @@
 ==Crystal structure of a mammalian reductase==
 <StructureSection load='2zat' size='340' side='right' caption='[[2zat]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbonyl_reductase_(NADPH) Carbonyl reductase (NADPH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.184 1.1.1.184] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zat OCA], [http://pdbe.org/2zat PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zat RCSB], [http://www.ebi.ac.uk/pdbsum/2zat PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2zat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zat OCA], [http://pdbe.org/2zat PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zat RCSB], [http://www.ebi.ac.uk/pdbsum/2zat PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zat ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/za/2zat_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/za/2zat_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2zat

From Proteopedia

Revision as of 09:10, 17 October 2018

Crystal structure of a mammalian reductase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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